An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions. - Suppr | 超能文献

An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions.

作者信息

Kerbiriou D, Hervé G

出版信息

J Mol Biol. 1973 Aug 25;78(4):687-702. doi: 10.1016/0022-2836(73)90289-1.

DOI:10.1016/0022-2836(73)90289-1

Abstract

摘要

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An aspartate transcarbamylase lacking catalytic subunit interactions. II. Regulatory subunits are responsible for the lack of co-operative interactions between catalytic sites. Drastic feedback inhibition does not restore these interactions.

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Subunit interactions in aspartate transcarbamylase. Characterization of a complex between the catalytic and the regulatory subunits.天冬氨酸转氨甲酰酶中的亚基相互作用。催化亚基与调节亚基之间复合物的特性研究。

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Co-operative interactions between the catalytic sites in Escherichia coli aspartate transcarbamylase. Role of the C-terminal region of the regulatory chains.大肠杆菌天冬氨酸转氨甲酰酶催化位点之间的协同相互作用。调节链C末端区域的作用。

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Changes in the hydrogen exchange kinetics of Escherichia coli aspartate transcarbamylase produced by effector binding and subunit association.效应物结合和亚基缔合对大肠杆菌天冬氨酸转氨甲酰酶氢交换动力学的影响。

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引用本文的文献

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Thermodynamics of assembly of Escherichia coli aspartate transcarbamoylase.大肠杆菌天冬氨酸转氨甲酰酶组装的热力学

Proc Natl Acad Sci U S A. 1983 Nov;80(22):6824-8. doi: 10.1073/pnas.80.22.6824.

2

A kinetic model of cooperativity in aspartate transcarbamylase.天冬氨酸转氨甲酰酶协同性的动力学模型。

Biophys J. 1977 Jun;18(3):245-67. doi: 10.1016/S0006-3495(77)85611-7.

3

Elimination of cooperativity in aspartate transcarbamylase by nitration of a single tyrosine residue.通过对单个酪氨酸残基进行硝化作用消除天冬氨酸转氨甲酰酶的协同性

Proc Natl Acad Sci U S A. 1978 Jun;75(6):2654-8. doi: 10.1073/pnas.75.6.2654.